Abstract
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amyloid / chemistry
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Amyloid beta-Peptides / chemistry*
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Binding Sites
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Chaperonin 60 / chemistry*
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Escherichia coli Proteins / chemistry*
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Humans
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Hydrophobic and Hydrophilic Interactions
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Kinetics
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Mapping
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Protein Structure, Secondary
Substances
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Amyloid
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Amyloid beta-Peptides
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Chaperonin 60
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Escherichia coli Proteins
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Peptide Fragments
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amyloid beta-protein (1-40)